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Literature summary for 2.3.2.B12 extracted from

  • Hänzelmann, P.; Stingele, J.; Hofmann, K.; Schindelin, H.; Raasi, S.
    The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain (2010), J. Biol. Chem., 285, 20390-20398.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of Ufd2 in complex with the ubiquitin-like (UBL) and ubiquitin-associated (UBA) proteins Rad23 and Dsk2 domains, PDB-ID: 3M62 and 3M63, respectively. The structure of Ufd2 is solved in complex with Rad23-UBL carrying either an N-terminal or a C-terminal His tag, refined at 2.4 A resolution. Ufd2 is composed of an N-terminal variable domain, a core domain, and a C-termional U-box with a fold similar to that of RING. The structure of Ufd2 with Dsk2-UBL is solved by molecular replacement. THe structure exhibits increased flexibility, in particular with a C-terminally tagged UBL domain. The N-terminal, tagged protein structure is refined at 2.4 A resolution. The N-terminal UBL-binding region of yeast Ufd2 is conserved on lower eukaryotes Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P54860 crystallization: structure of Ufd2 in complex with the ubiquitin-like (UBL) and ubiquitin-associated (UBA) proteins Rad23 and Dsk2 domains, PDB-ID: 3M62 and 3M63, respectively; S288c
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Saccharomyces cerevisiae ATCC 204508 P54860 crystallization: structure of Ufd2 in complex with the ubiquitin-like (UBL) and ubiquitin-associated (UBA) proteins Rad23 and Dsk2 domains, PDB-ID: 3M62 and 3M63, respectively; S288c
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Purification (Commentary)

Purification (Comment) Organism
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Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
E4 ubiquitin-protein ligase UFD2
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Saccharomyces cerevisiae
ubiquitin conjugation factor E4
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Saccharomyces cerevisiae
ubiquitin fusion degradation protein 2
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Saccharomyces cerevisiae
Ufd2
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Saccharomyces cerevisiae